Document Detail


Amyloid-associated nucleic acid hybridisation.
MedLine Citation:
PMID:  21625537     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Nucleic acids promote amyloid formation in diseases including Alzheimer's and Creutzfeldt-Jakob disease. However, it remains unclear whether the close interactions between amyloid and nucleic acid allow nucleic acid secondary structure to play a role in modulating amyloid structure and function. Here we have used a simplified system of short basic peptides with alternating hydrophobic and hydrophilic amino acid residues to study nucleic acid - amyloid interactions. Employing biophysical techniques including X-ray fibre diffraction, circular dichroism spectroscopy and electron microscopy we show that the polymerized charges of nucleic acids concentrate and enhance the formation of amyloid from short basic peptides, many of which would not otherwise form fibres. In turn, the amyloid component binds nucleic acids and promotes their hybridisation at concentrations below their solution K(d), as shown by time-resolved FRET studies. The self-reinforcing interactions between peptides and nucleic acids lead to the formation of amyloid nucleic acid (ANA) fibres whose properties are distinct from their component polymers. In addition to their importance in disease and potential in engineering, ANA fibres formed from prebiotically-produced peptides and nucleic acids may have played a role in early evolution, constituting the first entities subject to Darwinian evolution.
Authors:
Sebastian Braun; Christine Humphreys; Elizabeth Fraser; Andrea Brancale; Matthias Bochtler; Trevor C Dale
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2011-05-19
Journal Detail:
Title:  PloS one     Volume:  6     ISSN:  1932-6203     ISO Abbreviation:  PLoS ONE     Publication Date:  2011  
Date Detail:
Created Date:  2011-05-31     Completed Date:  2011-11-28     Revised Date:  2013-06-28    
Medline Journal Info:
Nlm Unique ID:  101285081     Medline TA:  PLoS One     Country:  United States    
Other Details:
Languages:  eng     Pagination:  e19125     Citation Subset:  IM    
Affiliation:
School of Biosciences, Cardiff University, Cardiff, Wales, United Kingdom.
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MeSH Terms
Descriptor/Qualifier:
Amyloid / chemistry*,  metabolism*
Amyloid beta-Peptides / chemistry*
Amyloid beta-Protein Precursor / antagonists & inhibitors
Circular Dichroism
Fluorescence Resonance Energy Transfer
Humans
Models, Molecular
Nucleic Acid Hybridization
Peptide Nucleic Acids / chemistry*,  metabolism*
Protein Binding
Protein Structure, Secondary
X-Ray Diffraction
Chemical
Reg. No./Substance:
0/APP protein, human; 0/Amyloid; 0/Amyloid beta-Peptides; 0/Amyloid beta-Protein Precursor; 0/Peptide Nucleic Acids
Comments/Corrections

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